ID   ZMIZ1_MOUSE             Reviewed;        1072 AA.
AC   Q6P1E1; Q6PDK9; Q6PF85; Q8BW47;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Zinc finger MIZ domain-containing protein 1;
DE   AltName: Full=PIAS-like protein Zimp10;
DE   AltName: Full=Retinoic acid-induced protein 17;
GN   Name=Zmiz1; Synonyms=Rai17, Zimp10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-416 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Ovary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=16862223; DOI=10.1621/nrs.04017;
RA   Beliakoff J., Sun Z.;
RT   "Zimp7 and Zimp10, two novel PIAS-like proteins, function as androgen
RT   receptor coregulators.";
RL   Nucl. Recept. Signal. 4:17-17(2006).
RN   [4]
RP   FUNCTION.
RX   PubMed=23161489; DOI=10.1158/0008-5472.can-12-1389;
RA   Rakowski L.A., Garagiola D.D., Li C.M., Decker M., Caruso S., Jones M.,
RA   Kuick R., Cierpicki T., Maillard I., Chiang M.Y.;
RT   "Convergence of the ZMIZ1 and NOTCH1 pathways at C-MYC in acute T
RT   lymphoblastic leukemias.";
RL   Cancer Res. 73:930-941(2013).
RN   [5]
RP   FUNCTION.
RX   PubMed=26522984; DOI=10.1016/j.immuni.2015.10.007;
RA   Pinnell N., Yan R., Cho H.J., Keeley T., Murai M.J., Liu Y., Alarcon A.S.,
RA   Qin J., Wang Q., Kuick R., Elenitoba-Johnson K.S., Maillard I.,
RA   Samuelson L.C., Cierpicki T., Chiang M.Y.;
RT   "The PIAS-like coactivator Zmiz1 is a direct and selective cofactor of
RT   Notch1 in T cell development and leukemia.";
RL   Immunity 43:870-883(2015).
RN   [6]
RP   INTERACTION WITH SMARCA4, AND TISSUE SPECIFICITY.
RX   PubMed=26163108; DOI=10.1007/s10048-015-0452-2;
RA   Cordova-Fletes C., Dominguez M.G., Delint-Ramirez I.,
RA   Martinez-Rodriguez H.G., Rivas-Estilla A.M., Barros-Nunez P.,
RA   Ortiz-Lopez R., Neira V.A.;
RT   "A de novo t(10;19)(q22.3;q13.33) leads to ZMIZ1/PRR12 reciprocal fusion
RT   transcripts in a girl with intellectual disability and neuropsychiatric
RT   alterations.";
RL   Neurogenetics 16:287-298(2015).
CC   -!- FUNCTION: Acts as a transcriptional coactivator. Increases ligand-
CC       dependent transcriptional activity of AR and promotes AR sumoylation.
CC       The stimulation of AR activity is dependent upon sumoylation (By
CC       similarity). Also functions as a transcriptional coactivator in the
CC       TGF-beta signaling pathway by increasing the activity of the
CC       SMAD3/SMAD4 transcriptional complex (By similarity). Involved in
CC       transcriptional activation of a subset of NOTCH1 target genes including
CC       MYC. Involved in thymocyte and T cell development (PubMed:26522984).
CC       Involved in the regulation of postmitotic positioning of pyramidal
CC       neurons in the developing cerebral cortex (By similarity).
CC       {ECO:0000250|UniProtKB:Q9ULJ6, ECO:0000269|PubMed:26522984}.
CC   -!- SUBUNIT: Interacts with AR, but not with ESR1, NR3C1, PGR, THRB nor
CC       VDR. Interacts with NOTCH1 and RBPJ (By similarity). Interacts with
CC       SMARCA4. Interacts (via SP-RING-type domain) with SMAD3 and SMAD4 (via
CC       MH2 domain) (By similarity). {ECO:0000250|UniProtKB:Q9ULJ6,
CC       ECO:0000269|PubMed:26163108}.
CC   -!- INTERACTION:
CC       Q6P1E1; Q3TKT4: Smarca4; NbExp=2; IntAct=EBI-647033, EBI-1210244;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000250|UniProtKB:Q9ULJ6}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9ULJ6}. Note=Enriched at replication foci
CC       throughout S phase. {ECO:0000250|UniProtKB:Q9ULJ6}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6P1E1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P1E1-2; Sequence=VSP_012187;
CC   -!- TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:26163108}.
CC   -!- DOMAIN: The C-terminal proline-rich domain possesses a significant
CC       intrinsic transcriptional activity. This activity is inhibited by the
CC       N-terminus in the full-length protein. {ECO:0000250|UniProtKB:Q9ULJ6}.
CC   -!- DOMAIN: The SP-RING-type domain mediates interaction with SMAD3 and
CC       SMAD4. {ECO:0000250|UniProtKB:Q9ULJ6}.
CC   -!- DISRUPTION PHENOTYPE: Death between 9.5-10.5 dpc. Mice are
CC       approximately half the size of wild-type littermates and display
CC       vascular and cell viability defects. Some heterozygotes also do not
CC       survive but those that do have no apparent defects.
CC       {ECO:0000269|PubMed:16862223}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC       site. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH57691.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC35753.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAC35753.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; BC057691; AAH57691.1; ALT_INIT; mRNA.
DR   EMBL; BC058646; AAH58646.1; -; mRNA.
DR   EMBL; BC065120; AAH65120.1; -; mRNA.
DR   EMBL; AK054366; BAC35753.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS26873.1; -. [Q6P1E1-1]
DR   CCDS; CCDS79280.1; -. [Q6P1E1-2]
DR   RefSeq; NP_001297595.1; NM_001310666.1. [Q6P1E1-2]
DR   RefSeq; NP_899031.2; NM_183208.4. [Q6P1E1-1]
DR   AlphaFoldDB; Q6P1E1; -.
DR   SMR; Q6P1E1; -.
DR   BioGRID; 236589; 1.
DR   IntAct; Q6P1E1; 5.
DR   STRING; 10090.ENSMUSP00000124863; -.
DR   iPTMnet; Q6P1E1; -.
DR   PhosphoSitePlus; Q6P1E1; -.
DR   EPD; Q6P1E1; -.
DR   MaxQB; Q6P1E1; -.
DR   PaxDb; 10090-ENSMUSP00000124863; -.
DR   PeptideAtlas; Q6P1E1; -.
DR   ProteomicsDB; 302065; -. [Q6P1E1-1]
DR   ProteomicsDB; 302066; -. [Q6P1E1-2]
DR   Pumba; Q6P1E1; -.
DR   Antibodypedia; 29855; 210 antibodies from 26 providers.
DR   DNASU; 328365; -.
DR   Ensembl; ENSMUST00000007961.15; ENSMUSP00000007961.9; ENSMUSG00000007817.16. [Q6P1E1-2]
DR   Ensembl; ENSMUST00000162645.8; ENSMUSP00000124863.2; ENSMUSG00000007817.16. [Q6P1E1-1]
DR   GeneID; 328365; -.
DR   KEGG; mmu:328365; -.
DR   UCSC; uc007srn.2; mouse. [Q6P1E1-1]
DR   UCSC; uc007sro.2; mouse. [Q6P1E1-2]
DR   AGR; MGI:3040693; -.
DR   MGI; MGI:3040693; Zmiz1.
DR   VEuPathDB; HostDB:ENSMUSG00000007817; -.
DR   eggNOG; KOG2169; Eukaryota.
DR   GeneTree; ENSGT01030000234539; -.
DR   HOGENOM; CLU_009461_1_0_1; -.
DR   InParanoid; Q6P1E1; -.
DR   OMA; PPMAMNQ; -.
DR   OrthoDB; 20246at2759; -.
DR   PhylomeDB; Q6P1E1; -.
DR   TreeFam; TF316952; -.
DR   BioGRID-ORCS; 328365; 8 hits in 78 CRISPR screens.
DR   ChiTaRS; Zmiz1; mouse.
DR   PRO; PR:Q6P1E1; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q6P1E1; Protein.
DR   Bgee; ENSMUSG00000007817; Expressed in humerus cartilage element and 247 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0030374; F:nuclear receptor coactivator activity; IBA:GO_Central.
DR   GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR   GO; GO:0061665; F:SUMO ligase activity; IBA:GO_Central.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030521; P:androgen receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0048844; P:artery morphogenesis; IMP:MGI.
DR   GO; GO:0090398; P:cellular senescence; IDA:MGI.
DR   GO; GO:0048589; P:developmental growth; IMP:MGI.
DR   GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
DR   GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:UniProtKB.
DR   GO; GO:0045582; P:positive regulation of T cell differentiation; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR   GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
DR   GO; GO:0021852; P:pyramidal neuron migration to cerebral cortex; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0060395; P:SMAD protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR   GO; GO:0007296; P:vitellogenesis; IMP:MGI.
DR   CDD; cd16822; SP-RING_ZMIZ1; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR040797; Zmiz1_N.
DR   InterPro; IPR004181; Znf_MIZ.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10782; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10782:SF7; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF02891; zf-MIZ; 1.
DR   Pfam; PF18028; Zmiz1_N; 1.
DR   PROSITE; PS51044; ZF_SP_RING; 1.
DR   Genevisible; Q6P1E1; MM.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Cytoplasm; Isopeptide bond; Metal-binding;
KW   Nucleus; Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..1072
FT                   /note="Zinc finger MIZ domain-containing protein 1"
FT                   /id="PRO_0000218988"
FT   ZN_FING         734..815
FT                   /note="SP-RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT   REGION          1..120
FT                   /note="Sufficient for transactivation activity; sufficient
FT                   for interaction with NOTCH1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULJ6"
FT   REGION          112..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          844..1072
FT                   /note="Transactivation domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULJ6"
FT   REGION          875..1072
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..450
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..538
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        888..905
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        952..974
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        984..1002
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1007..1023
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1055..1072
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         765
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT   BINDING         767
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT   BINDING         788
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT   BINDING         791
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT   CROSSLNK        91
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULJ6"
FT   CROSSLNK        841
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULJ6"
FT   CROSSLNK        850
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULJ6"
FT   VAR_SEQ         320..325
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_012187"
SQ   SEQUENCE   1072 AA;  115851 MW;  53B1AF1338EBDB17 CRC64;
     MNSMDRHIQQ TNDRLQCIKQ HLQNPANFHN AATELLDWCG DPRAFQRPFE QSLMGCLTVV
     SRVAAQQGFD LDLGYRLLAV CAANRDKFTP KSAALLSSWC EELGRLLLLR HQKSRQNDPP
     GKLPMQPPLS SMSSMKPTLS HSDGSFPYDS VPWQQNTNQP PGSLSVVTTV WGVTNTSQSQ
     VLGNPMANAN NPMNPGGNPM ASGMSTSNPG INSPQFAGQQ QQFSTKAGPA QPYIQPNMYG
     RPGYPGSGGF GASYPGGPSA PAGMGIPPHT RPPADFTQPA AAAAAAAVAA AAATATATAT
     ATVAALQETQ NKDINQYGPV CSSFQMGPTQ AYNSQFMNQP GPRGPASMGG SLNPAGMAAG
     MTPSGMSGPP MGMNQPRPPG ISPFGTHGQR MPQQTYPGPR PQSLPIQSIK RPYPGEPNYG
     NQQYGPNSQF PTQPGQYPTP NPPRPLTSPN YPGQRMPSQP STGQYPPPTV NMGQYYKPEQ
     FNGQNNTFSS GSSYSSYSQG SVNRPPRPVP VANYPHSPVP GNPTPPMTPG SSIPPYLSPS
     QDVKPPFPPD IKPNMSALPP PPANHNDELR LTFPVRDGVV LEPFRLEHNL AVSNHVFHLR
     PTVHQTLMWR SDLELQFKCY HHEDRQMNTN WPASVQVSVN ATPLTIERGD NKTSHKPLHL
     KHVCQPGRNT IQITVTACCC SHLFVLQLVH RPSVRSVLQG LLKKRLLPAE HCITKIKRNF
     SSVAASSGNT TLNGEDGVEQ TAIKVSLKCP ITFRRIQLPA RGHDCKHVQC FDLESYLQLN
     CERGTWRCPV CNKTALLEGL EVDQYMWGIL NAIQHSEFEE VTIDPTCSWR PVPIKSDLHI
     KDDPDGIPSK RFKTMSPSQM IMPNVMEMIA ALGPGPSPYP LPPPPGGTSS NDYSSQGNNY
     QGHGNFDFPH GNPGGTSMND FMHGPPQLSH PPDMPNNMAA LEKPLSHPMQ ETMPHAGSSD
     QPHPSIQQGL HVPHPSSQAG PPLHHSGAPP PSQPPRQPPQ AAPGNHPHSD LTFNPSSALE
     GQAGAQGASD MPEPSLDLLP ELTNPDELLS YLDPPDLPSN SNDDLLSLFE NN
//